ID Q6MS43_MYCMS Unreviewed; 310 AA.
AC Q6MS43;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN Name=trxB {ECO:0000313|EMBL:CAE77547.1};
GN OrderedLocusNames=MSC_0938 {ECO:0000313|EMBL:CAE77547.1};
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632 {ECO:0000313|EMBL:CAE77547.1, ECO:0000313|Proteomes:UP000001016};
RN [1] {ECO:0000313|EMBL:CAE77547.1, ECO:0000313|Proteomes:UP000001016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1 {ECO:0000313|EMBL:CAE77547.1,
RC ECO:0000313|Proteomes:UP000001016};
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000256|RuleBase:RU003880};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU003880};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003880}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|RuleBase:RU003880}.
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DR EMBL; BX293980; CAE77547.1; -; Genomic_DNA.
DR RefSeq; NP_975905.1; NC_005364.2.
DR AlphaFoldDB; Q6MS43; -.
DR STRING; 272632.MSC_0938; -.
DR KEGG; mmy:MSC_0938; -.
DR PATRIC; fig|272632.4.peg.1020; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_3_14; -.
DR Proteomes; UP000001016; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR NCBIfam; TIGR01292; TRX_reduct; 1.
DR PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003880};
KW Flavoprotein {ECO:0000256|RuleBase:RU003880};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003880};
KW Redox-active center {ECO:0000256|RuleBase:RU003880};
KW Reference proteome {ECO:0000313|Proteomes:UP000001016}.
FT DOMAIN 9..291
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 310 AA; 33504 MW; E5BF4A572BF82132 CRC64;
MKNLTNEIYD VIIVGSGPAG LTSAIYTARA GLKTVIYEQS APGGKLIKTD LIENYPGFET
IQGPDLASKM YLQALSLNAS VEFVGVDSIF KNADDIFEIS LTNGEIKKAY SVILATGTQE
NKLGIKGEDE LYGKGVSYCA VCDGAFYKNK PVAVVGGGYS AVQEAMYLSQ LVDKVYLIVR
RDVFRADANK VAKLKAQPNV EFLLKSQVKE IHGAEKVESL TITTPDGEKK LVVSAIFPYI
GSTPLIDSVK HLCIENEKGY IPTNDKMQTE IKGLFVAGDV RDVPLRQIAI ACGDGAIAGQ
MAVEYVQEVK
//
